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Fig. 1. E-cadherin constructs that do not bind β-catenin accumulate in intracellular compartments in MDCK cells. (A) Schematic representations of HA-tagged wild-type E-cadherin (Ecad) and two Ecad mutants: ESA, full-length E-cadherin in which eight conserved serine residues within the catenin-binding site are substituted with alanine; EC81, E-cadherin in which 70 amino acids of the C-terminal are deleted. (B) Immunofluorescence staining of MDCK cells immunostained for Ecad, ESA and EC81 using anti-HA mAbs. Analysis of two to four other clones expressing each construct gave essentially the same results. (C) Trypsin digestion of cells expressing Ecad, ESA or EC81 with or without free Ca²⁺. Cells were incubated with 0.01% trypsin for 10 minutes at 37°C in the presence of 2 mM Ca²⁺ (TC) or 1 mM EGTA (TE) and immunostaining with anti-HA mAb showed that a significant percentage of ESA and EC81 remain inside the cells. Protein bands of high molecular mass (marked by asterisks) correspond to the intracellular, incompletely processed proteins that retain the precursor segment.

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